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J. Biol. Chem., Vol. 281, Issue 26, 17541-17544, June 30, 2006

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Minireview

Inhibiting Bacterial Fatty Acid Synthesis^*

Yong-Mei Zhang, Stephen W. White, and Charles O. Rock¹

From the Departments of Infectious Diseases and Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-2794

The type II fatty acid synthase consists of a series of individual enzymes, each encoded by a separate gene, that catalyze discrete steps in chain elongation. The formation of fatty acids is vital to bacteria, and each of the essential enzymes and their acyl group carriers represent a potential target for the development of novel antibacterial therapeutics. High resolution x-ray and/or NMR structures of representative members of every enzyme in the type II pathway are now available, and these structures are a valuable resource to guide antibacterial drug discovery. The role of each enzyme in regulating pathway activity and the diversity in the components of the pathway in the major human pathogens are important considerations in deciding the most suitable targets for future drug development.

^* This minireview will be reprinted in the 2006 Minireview Compendium, which will be available in January, 2007. This work was supported by National Institutes of Health Grant GM34496 (to C. O. R.), Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Syrian Associated Charities.

¹ To whom correspondence should be addressed: Dept. of Infectious Diseases, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Tel.: 901-495-3491; Fax: 901-495-3099; E-mail: charles.rock{at}stjude.org.

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